Resolution of inflammation, an active process that prevents damage to the host and re-establishes homeostasis, is governed by specific mediators (Serhan, C. N., S. D. Brain, C. D. Buckley, D. W. Gilroy, C. Haslett, L. A. O'Neill, M. Perretti, A. G. Rossi, and J. L. Wallace. 2007. Resolution of inflammation: state of the art, definitions and terms. FASEB J 21:325-332). Among these, the arachidonic acid (AA)-derived lipoxins (LX), an acronym for lipoxygenase (LO)-interaction-products, were the first autacoids recognized to carry dual antiinflammatory and pro-resolution activities (Maderna, P., and C. Godson. 2009. Lipoxins: resolutionary road. Br J Pharmacol 158:947-959; Serhan, C. N., M. Hamberg, and B. Samuelsson. 1984a. Lipoxins: novel series of biologically active compounds formed from arachidonic acid in human leukocytes. Proc Natl Acad Sci USA 81:5335-5339; Serhan, C. N., M. Hamberg, and B. Samuelsson. 1984b. Trihydroxytetraenes: a novel series of compounds formed from arachidonic acid in human leukocytes. Biochem Biophys Res Commun 118:943-949). LXA4 (5,6,155-trihydroxy-7,9,11,13-trans-1′-cis-eicosatetraenoic acid) is biosynthesized during cell-cell interactions by transcellular metabolic routes involving 5-LO and 12- or 15-LO (Maderna, P., and C. Godson. 2009. Lipoxins: resolutionary road. Br J Pharmacol 158:947-959; Romano, M. 2010. Lipoxin and aspirin-triggered lipoxins. ScientificWorldJournal 10:1048-1064). Within the vasculature, different pathways lead to the biosynthesis of LX. During platelet-leukocyte interactions, leukotriene (LT)A4 released from leukocytes is converted into LXA4 and B4 by platelet 12-LO (Romano, M., and C. N. Serhan. 1992. Lipoxin generation by permeabilized human platelets. Biochemistry 31:8269-8277; Romano, M., X. S. Chen, Y. Takahashi, S. Yamamoto, C. D. Funk, and C. N. Serhan. 1993. Lipoxin synthase activity of human platelet 12-lipoxygenase. Biochem J 296 (Pt 1):127-133). In addition, aspirin, a widely used anti-inflammatory and anti-thrombotic drug, promotes the biosynthesis of 015 epimers of LX (5,6,15R-trihydroxy-7,9,11,13-trans-11-cis-eicosatetraenoic acid), also termed “aspirin triggered” LX (ATL) via acetylation of endothelial cyclooxygenase-2 (COX-2) (Claria, J., and C. N. Serhan. 1995. Aspirin triggers previously undescribed bioactive eicosanoids by human endothelial cell-leukocyte interactions. Proc Natl Acad Sci USA 92:9475-9479). ATL proved to mediate the anti-inflammatory actions of low-dose aspirin in humans, independently from inhibition of prostanoid biosynthesis (Morris, T., M. Stables, A. Hobbs, P. de Souza, P. Colville-Nash, T. Warner, J. Newson, G. Bellingan, and D. W. Gilroy. 2009. Effects of low-dose aspirin on acute inflammatory responses in humans. J Immunol 183:2089-2096). Importantly, statins, through the S-nitrosilation of COX-2, also trigger the generation of 15-epi-LXA4 (Birnbaum, Y., Y. Ye, Y. Lin, S. Y. Freeberg, S. P. Nishi, J. D. Martinez, M. H. Huang, B. F. Uretsky, and J. R. Perez-Polo. 2006. Augmentation of myocardial production of 15-epi-lipoxin-a4 by pioglitazone and atorvastatin in the rat. Circulation 114:929-935; Planaguma, A., M. A. Pfeffer, G. Rubin, R. Croze, M. Uddin, C. N. Serhan, and B. D. Levy. 2010. Lovastatin decreases acute mucosal inflammation via 15-epi-lipoxin A4. Mucosal Immunol 3:270-279). LXA4 and ATL modulate the immune-inflammatory response by inhibiting polymorphonuclear leukocyte (PMN) infiltration in inflamed tissues and stimulating phagocytosis of apoptotic PMN and microbes (Maderna, P., and C. Godson. 2009. Lipoxins: resolutionary road. Br J Pharmacol 158:947-959) in vivo, thus promoting resolution. Moreover, they display potent protective actions in the cardiovascular district, by directly stimulating the production of prostacyclin and nitric oxide, upregulating heme oxygenase-1, and reducing oxidative stress in endothelial cells (Maderna, P., and C. Godson. 2009. Lipoxins: resolutionary road. Br J Pharmacol 158:947-959).
LXA4 and ATL exert their bioactions by activating a specific G-protein-coupled receptor (GPCR). Initially reported as a structural homologue of the N-formyl peptide receptor and termed formyl peptide receptor like-1 (FPRL1) (Murphy, P. M., T. Ozcelik, R. T. Kenney, H. L. Tiffany, D. McDermott, and U. Francke. 1992. A structural homologue of the N-formyl peptide receptor. Characterization and chromosome mapping of a peptide chemoattractant receptor family. J Biol Chem 267:7637-7643; Perez, H. D., R. Holmes, E. Kelly, J. McClary, and W. H. Andrews. 1992. Cloning of a cDNA encoding a receptor related to the formyl peptide receptor of human neutrophils. Gene 118:303-304; Ye, R. D., S. L. Cavanagh, O. Quehenberger, E. R. Prossnitz, and C. G. Cochrane. 1992. Isolation of a cDNA that encodes a novel granulocyte N-formyl peptide receptor. Biochem Biophys Res Commun 184:582-589) it was later identified as the LXA4 receptor in human leukocytes (Fiore, S., J. F. Maddox, H. D. Perez, and C. N. Serhan. 1994. Identification of a human cDNA encoding a functional high affinity lipoxin A4 receptor. J Exp Med 180:253-260). The most recent nomenclature has renamed this receptor FPR2/ALX in light of its high affinity for LXA4 (Ye, R. D., F. Boulay, J. M. Wang, C. Dahlgren, C. Gerard, M. Parmentier, C. N. Serhan, and P. M. Murphy. 2009. International Union of Basic and Clinical Pharmacology. LXXIII. Nomenclature for the formyl peptide receptor (FPR) family. Pharmacol Rev 61:119-161). The FPR2/ALX gene (Bao, L., N. P. Gerard, R. L. Jr Eddy, T. B. Shows, and C. Gerard. 1992. Mapping of genes for the human C5a receptor (CSAR), human FMLP receptor (FPR), and two FMLP receptor homologue orphan receptors (FPRH1, FPRH2) to chromosome 19. Genomics 13:437-440) is located on chromosome 19. It spans 9.6 kb and encompasses two exons and two introns. Alternative splicing produces four different transcripts, which encode the same seven transmembrane domain protein of 351 aminoacids. Human FPR2/ALX is highly expressed in myeloid cells and at a lower extent in lymphocytes, endothelial and epithelial cells (Romano, M., I. Recchia, and A. Recchiuti. 2007. Lipoxin receptors. ScientificWorldJournal 7:1393-1412). Orthologues of the human FPR2/ALX have been identified in the mouse (Takano, T., S. Fiore, J. F. Maddox, H. R. Brady, N. A. Petasis, and C. N. Serhan. 1997. Aspirin-triggered 15-epi-lipoxin A4 (LXA4) and LXA4 stable analogues are potent inhibitors of acute inflammation: evidence for anti-inflammatory receptors. J Exp Med 185:1693-1704) and rat (Chiang, N., T. Takano, M. Arita, S. Watanabe, and C. N. Serhan. 2003. A novel rat lipoxin A4 receptor that is conserved in structure and function. Br J Pharmacol 139:89-98). In addition to LXA4, FPR2/ALX is activated by the glucocorticoid-induced protein annexin-1 and its N-terminal peptides (Ferretti, M., N. Chiang, M. La, I. M. Fierro, S. Marullo, S. J. Getting, E. Solito, and C. N. Serhan. 2002. Endogenous lipid- and peptide-derived anti-inflammatory pathways generated with glucocorticoid and aspirin treatment activate the lipoxin A4 receptor. Nat Med 8:1296-1302), representing the first identified GPCR able to mediate anti-inflammatory and pro-resolving actions of both lipid and peptide endogenous mediators. Recently, activation of FPR2/ALX by the omega 3-derived pro-resolution mediator, Resolvin D1 has been reported (Krishnamoorthy, S., A. Recchiuti, N. Chiang, S. Yacoubian, C. H. Lee, R. Yang, N. A. Petasis, and C. N. Serhan. 2010. Resolvin D1 binds human phagocytes with evidence for proresolving receptors. Proc Natl Acad Sci USA 107:1660-1665) further supporting the relevance of this receptor in inflammation resolution. On the other hand, FPR2/ALX can trigger pro-inflammatory signaling when activated by some microbial and mitochondrial peptides (Romano, M., I. Recchia, and A. Recchiuti. 2007. Lipoxin receptors. ScientificWorldJournal 7:1393-1412) raising the question of its pathophysiological significance in vivo. This question has been addressed by gene manipulation studies. Overexpression of human FPR2/ALX in myeloid cells of transgenic mice reduced neutrophil infiltration in a model of zymosan-induced peritonitis in vivo in the absence of exogenously added agonists (Devchand, P. R., M. Arita, S. Hong, G. Bannenberg, R. L. Moussignac, K. Gronert, and C. N. Serhan. 2003. Human ALX receptor regulates neutrophil recruitment in transgenic mice: roles in inflammation and host defense. FASEB J 17:652-659). Moreover, genetic deletion of the murine orthologue of human FPR2/ALX resulted in a more pronounced inflammatory phenotype, with lack of resolution and no response to annexin 1 and LXA4 (Dutton, N., R. Hannon, V. Brancaleone, J. Dalli, H. B. Patel, M. Gray, F. D'Acquisto, J. C. Buckingham, M. Perretti, and R. J. Flower. 2010. Anti-inflammatory role of the murine formyl-peptide receptor 2: ligand-specific effects on leukocyte responses and experimental inflammation. J Immuno/184:2611-2619). Along these lines, 15-epi-LXA4 biosynthesis and FPR2/ALX expression determine the magnitude and duration of the inflammatory reaction in humans (Morris, T., M. Stables, P. Colville-Nash, J. Newson, G. Bellingan, P. M. de Souza, and D. W. Gilroy. 2010. Dichotomy in duration and severity of acute inflammatory responses in humans arising from differentially expressed proresolution pathways. Proc Natl Aced Sci USA 107:8842-8847). Furthermore, decreased LXA4 biosynthesis and FPR2/ALX expression have been observed in asthmatic patients (Levy, B. D., C. Bonnans, E. S. Silverman, L. J. Palmer, G. Marigowda, and E. Israel. 2005. Diminished lipoxin biosynthesis in severe asthma. Am J Respir Crit. Care Med 172:824-830; Planaguma, A., S. Kazani, G. Marigowda, O. Haworth, T. J. Mariani, E. Israel, E. R. Bleecker, D. Curran-Everett, S. C. Erzurum, W. J. Calhoun, M. Castro, K. F. Chung, B. Gaston, N, N. Jarjour, W. W. Busse, S. E. Wenzel, and B. D. Levy. 2008. Airway lipoxin A4 generation and lipoxin A4 receptor expression are decreased in severe asthma. Am J Respir Crit Care Med 178:574-582). These observations support the anti-inflammatory, pro-resolution function of the LXA4-FPR2/ALX axis, whose impairment may represent an underlying pathogenetic mechanism of inflammatory chronic diseases.
WO2005047899, Nash e al., in the name of ACADIA PHARMACEUTICALS, INC published on 26 May 2005 discloses selective agonists of FPRL1 receptor of general formula:

For the treatment of inflammatory conditions and their use for selecting anti-inflammatory and analgesic drugs.
US2002052529 published on 16 May 2002 and the corresponding international application WO2001068839 in the name of BAYER AKTIENGESELLSCHAFT published on 20 Sep. 2001 disclose nucleotide sequences encoding for a lipoxin A4 receptor-like polypeptide.
Examples of drug screening methods are disclosed for example in WO2002020759 and WO2003102026.
U.S. Pat. No. 6,245,512 discloses the cloning and characterization of the VEGF receptor gene promoter (Flt-1).